Department of Biomedical Engineering, University of Saskatchewan, Saskatoon S7N5A9, Canada.
Nanotechnology. 2011 Apr 8;22(14):145703. doi: 10.1088/0957-4484/22/14/145703. Epub 2011 Feb 24.
In the present research, the conformation of bovine serum albumin (BSA) in the nanodiamond particle (ND)-BSA complex was studied by Fourier transform infrared spectroscopy, fluorescence spectroscopy, UV-vis spectroscopy, and circular dichroism spectroscopy. The spectroscopic study revealed that most BSA structural features could be preserved in the complex though the BSA underwent conformational changes in the complex due to ND-BSA interaction. In addition, BSA adsorption isotherms and zeta-potential measurements were employed to investigate the pH dependence of the ND-BSA interaction. The changes in surface charge of the ND-BSA complex with pH variations indicated that the binding of BSA to ND might lead to not only the adsorption of BSA onto the ND surface but also the partial breakup of ND aggregates into relatively small ND-BSA aggregates because of the strong binding force between ND and BSA. The results show that ND is an excellent platform for protein immobilization with high affinity and holds great potential to be used for biosensor applications.
在本研究中，通过傅里叶变换红外光谱、荧光光谱、紫外可见光谱和圆二色光谱研究了纳米金刚石颗粒（ND）-BSA 复合物中牛血清白蛋白（BSA）的构象。光谱研究表明，尽管由于 ND-BSA 相互作用，BSA 在复合物中发生构象变化，但BSA 的大多数结构特征在复合物中得以保留。此外，还采用 BSA 吸附等温线和 zeta 电位测量研究了 ND-BSA 相互作用的 pH 依赖性。ND-BSA 复合物表面电荷随 pH 变化的变化表明，BSA 与 ND 的结合不仅可能导致 BSA 吸附到 ND 表面，而且由于 ND 和 BSA 之间的强结合力，ND 聚集体可能部分分解成相对较小的 ND-BSA 聚集体。结果表明，ND 是一种具有高亲和力的蛋白质固定的优异平台，具有很大的潜力可用于生物传感器应用。
